ID   CT32_CONLI              Reviewed;          61 AA.
AC   Q3YEH5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Conotoxin LiC32 {ECO:0000303|PubMed:16999774};
DE   Flags: Precursor;
OS   Conus lividus (Livid cone).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Neogastropoda; Conoidea; Conidae; Conus; Lividoconus.
OX   NCBI_TaxID=89426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT CYS-60.
RC   TISSUE=Venom duct;
RX   PubMed=16999774; DOI=10.1111/j.1747-0285.2006.00422.x;
RA   Luo S., Zhangsun D., Wu Y., Zhu X., Xie L., Hu Y., Zhang J., Zhao X.;
RT   "Identification and molecular diversity of T-superfamily conotoxins from
RT   Conus lividus and Conus litteratus.";
RL   Chem. Biol. Drug Des. 68:97-106(2006).
RN   [2]
RP   FUNCTION, AND SYNTHESIS OF 46-60.
RX   PubMed=23567999; DOI=10.1016/j.bcp.2013.03.019;
RA   Petrel C., Hocking H.G., Reynaud M., Upert G., Favreau P., Biass D.,
RA   Paolini-Bertrand M., Peigneur S., Tytgat J., Gilles N., Hartley O.,
RA   Boelens R., Stocklin R., Servent D.;
RT   "Identification, structural and pharmacological characterization of tau-
RT   CnVA, a conopeptide that selectively interacts with somatostatin sst
RT   receptor.";
RL   Biochem. Pharmacol. 85:1663-1671(2013).
CC   -!- FUNCTION: Has the ability to interact with the G-protein coupled
CC       somatostatin type 3 receptor (SSTR3). The ability was measured in
CC       competition binding experiments and the constant of inhibition (Ki) has
CC       been evaluated to be 3.5 uM. {ECO:0000269|PubMed:23567999}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- DOMAIN: The cysteine framework is V (CC-CC).
CC   -!- PTM: Contains 2 disulfide bonds that can be either 'C1-C3, C2-C4' or
CC       'C1-C4, C2-C3', since these disulfide connectivities have been observed
CC       for conotoxins with cysteine framework V (for examples, see AC P0DQQ7
CC       and AC P81755). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the conotoxin T superfamily. {ECO:0000305}.
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DR   EMBL; DQ141138; AAZ85403.1; -; mRNA.
DR   AlphaFoldDB; Q3YEH5; -.
DR   ConoServer; 1675; LiC32 precursor.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR031565; T-conotoxin.
DR   Pfam; PF16981; Chi-conotoxin; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Disulfide bond;
KW   G-protein coupled receptor impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..44
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000274057"
FT   PEPTIDE         46..60
FT                   /note="Conotoxin LiC32"
FT                   /id="PRO_0000274058"
FT   MOD_RES         60
FT                   /note="Cysteine amide"
FT                   /evidence="ECO:0000269|PubMed:16999774"
SQ   SEQUENCE   61 AA;  6976 MW;  C7EDF61EB51FD768 CRC64;
     MRCVPVFIIL LLLSPSAPSV DAHPKTKDDV PLASFHDDAK RTLQRLWQNT WCCRDHLRCC
     G